4epc

Crystal structure of Autolysin repeat domains from Staphylococcus epidermidis

spinqualitylabelsall models 4epc, resolution 2.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4epc is a 1 chain structure with sequence from Staphylococcus epidermidis. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.9Å Ligands: MLY Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function ATL_STAEP Publication Abstract from PubMed The bifunctional major autolysin Atl plays a key role in staphylococcal cell separation. Processing of Atl yields catalytically active amidase (AM) and glucosaminidase (GL) domains that are each fused to repeating units. The two repeats of AM (R1 and R2) target the enzyme to the septum, where it cleaves murein between dividing cells. We have determined the crystal structure of R2, which reveals that each repeat folds into two half-open beta-barrel subunits. We furthermore demonstrate that lipoteichoic acid serves as a receptor for the repeats, and that this interaction depends on conserved surfaces in each subunit. Small angle X-ray scattering of the mature amidase reveals the presence of flexible linkers separating the AM, R1 and R2 units. Different levels of flexibility for each linker provide mechanistic insights into the conformational dynamics of the full-length protein and the roles of its components in cell wall association and catalysis. Our analysis supports a model in which the repeats direct the catalytic AM domain to the septum, where it can optimally perform the final step of cell division. Ligand-binding properties and conformational dynamics of autolysin repeat domains in staphylococcal cell wall recognition.,Zoll S, Schlag M, Shkumatov AV, Rautenberg M, Svergun DI, Gotz F, Stehle T J Bacteriol. 2012 May 18. PMID:22609916 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA